Evidence map›Paper›PMID 22891241›Full record

ArticleThe Journal of biological chemistry2012

Ezrin/radixin/moesin are required for the purinergic P2X7 receptor (P2X7R)-dependent processing of the amyloid precursor protein.

Amaria Darmellah, Amel Rayah, Rodolphe Auger, Marie-Hélène Cuif, Magali Prigent, Monique Arpin, Andres Alcover, Cécile Delarasse, Jean M Kanellopoulos

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. The P2X7 Receptor, a Multifaceted Receptor in Alzheimer's Disease.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. The Role of P2X7 Receptor in Alzheimer's Disease.Frontiers in molecular neuroscience · 2020
    Review
  10. Review
  11. Pleiotropic Roles of P2X7 in the Central Nervous System.Frontiers in cellular neuroscience · 2019
    Review
  12. Article
  13. Article
  14. Roles of extracellular nucleotides and P2 receptors in ectodomain shedding.Cellular and molecular life sciences : CMLS · 2016
    Review
  15. Central Role of P2Y6 UDP Receptor in Arteriolar Myogenic Tone.Arteriosclerosis, thrombosis, and vascular biology · 2016
    Article
  16. Article
  17. Article
  18. Review
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Amaria DarmellahInstitut de Biochimie et Biophysique Moléculaire et Cellulaire, CNRS UMR 8619, France.
Amel Rayah
Rodolphe Auger
Marie-Hélène Cuif
Magali Prigent
Monique Arpin
Andres Alcover
Cécile Delarasse
Jean M Kanellopoulos
Centre National de la Recherche Scientifique · FRInstitut de Biochimie et Biophysique Moléculaire et Cellulaire · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amyloid precursor protein (APP) can be cleaved by α-secretases in neural cells to produce the soluble APP ectodomain (sAPPα), which is neuroprotective. We have shown previously that activation of the purinergic P2X7 receptor (P2X7R) triggers sAPPα shedding from neural cells. Here, we demonstrate that the activation of ezrin, radixin, and moesin (ERM) proteins is required for the P2X7R-dependent proteolytic processing of APP leading to sAPPα release. Indeed, the down-regulation of ERM by siRNA blocked the P2X7R-dependent shedding of sAPPα. We also show that P2X7R stimulation triggered the phosphorylation of ERM. Thus, ezrin translocates to the plasma membrane to interact with P2X7R. Using specific pharmacological inhibitors, we established the order in which several enzymes trigger the P2X7R-dependent release of sAPPα. Thus, a Rho kinase and the MAPK modules ERK1/2 and JNK act upstream of ERM, whereas a PI3K activity is triggered downstream. For the first time, this work identifies ERM as major partners in the regulated non-amyloidogenic processing of APP.

Indexed as

ProteolysisAmyloid beta-Protein PrecursorAnimalsCell Line, TumorCytoskeletal ProteinsEzrinHEK293 CellsHumansMembrane ProteinsMiceMicrofilament ProteinsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Phosphatidylinositol 3-KinasesReceptors, Purinergic P2X7rho-Associated KinasesAmyloid beta-Protein PrecursorAPP protein, humanCytoskeletal ProteinsEzrinMAPK1 protein, humanMembrane ProteinsMicrofilament ProteinsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3moesinPhosphatidylinositol 3-KinasesradixinReceptors, Purinergic P2X7rho-Associated Kinases

Identifiers

PMID22891241
PMCPMC3464564
OpenAlexW1971870999

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.